Evidence map›Paper›PMID 30678096›Full record

ReviewAntioxidants (Basel, Switzerland)2019

Signals Getting Crossed in the Entanglement of Redox and Phosphorylation Pathways: Phosphorylation of Peroxiredoxin Proteins Sparks Cell Signaling.

John J Skoko, Shireen Attaran, Carola A Neumann

Open access · goldAbstract readReview
In one paragraph

Review in Antioxidants (Basel, Switzerland), 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.

0numbers the graph read from it
0cells of the map it votes in
14citing papers in PubMed
1.4field-weighted citation impact, top 19% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

14 citing papers in PubMed, 25 citations in OpenAlex.

  1. Article
  2. Review
  3. Review
  4. Reactive oxygen species: role in obesity and mitochondrial energy efficiency.Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2023
    Review
  5. Review
  6. Effects of Date Palm Pollen Supplementations on The Expression ofInternational journal of fertility & sterility · 2023
    Article
  7. Article
  8. Article
  9. Review
  10. Article
  11. In vivo observation of peroxiredoxins oligomerization dynamics.Proceedings of the National Academy of Sciences of the United States of America · 2020
    Article
  12. Real-time monitoring of peroxiredoxin oligomerization dynamics in living cells.Proceedings of the National Academy of Sciences of the United States of America · 2020
    Article
  13. Oxidative Stress: A Unifying Paradigm in Hypertension.The Canadian journal of cardiology · 2020
    Review
  14. Review
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

3 authors at 2 institutions in 1 country.

John J SkokoDepartment of Pharmacology and Chemical Biology, School of Medicine, University of Pittsburgh, Pittsburgh, PA 15261, USA. jskoko@pitt.edu.
Shireen AttaranDepartment of Pharmacology and Chemical Biology, School of Medicine, University of Pittsburgh, Pittsburgh, PA 15261, USA. sha60@pitt.edu.
Carola A NeumannDepartment of Pharmacology and Chemical Biology, School of Medicine, University of Pittsburgh, Pittsburgh, PA 15261, USA. neumannc@upmc.edu.
Cancer Research Center · USMagee-Womens Research Institute · US

Funding

VECTOR CORE FACILITYP30CA047904 · NCI · UNIVERSITY OF PITTSBURGH AT PITTSBURGH · PI JOHN C. BYRD · 1988 to 2026
$158.0M
The Role of Peroxiredoxin1 & Reactive Oxygen Species in Breast Tumor InitiationR01CA131350 · NCI · UNIVERSITY OF PITTSBURGH AT PITTSBURGH · PI NEUMANN, CAROLA ANKE · 2010 to 2014
$1.5M
Howard Hughes Medical Institute Gilliam predoctoral fellowshipNCI NIH HHS P30 CA047904NCI NIH HHS R01 CA131350NIH HHS CA131350
6 · The paper itself

Abstract

Reactive oxygen and nitrogen species have cell signaling properties and are involved in a multitude of processes beyond redox homeostasis. The peroxiredoxin (Prdx) proteins are highly sensitive intracellular peroxidases that can coordinate cell signaling via direct reactive species scavenging or by acting as a redox sensor that enables control of binding partner activity. Oxidation of the peroxidatic cysteine residue of Prdx proteins are the classical post-translational modification that has been recognized to modulate downstream signaling cascades, but increasing evidence supports that dynamic changes to phosphorylation of Prdx proteins is also an important determinant in redox signaling. Phosphorylation of Prdx proteins affects three-dimensional structure and function to coordinate cell proliferation, wound healing, cell fate and lipid signaling. The advent of large proteomic datasets has shown that there are many opportunities to understand further how phosphorylation of Prdx proteins fit into intracellular signaling cascades in normal or malignant cells and that more research is necessary. This review summarizes the Prdx family of proteins and details how post-translational modification by kinases and phosphatases controls intracellular signaling.

Indexed as

cell signalingperoxiredoxinphosphorylationPrdxPrxredox signaling

Identifiers

PMID30678096
PMCPMC6406269
OpenAlexW2911742017

What OpenQuestion holds

Textmetadata
LicenceCC BY
Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.